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Q8WYB5

- KAT6B_HUMAN

UniProt

Q8WYB5 - KAT6B_HUMAN

Protein

Histone acetyltransferase KAT6B

Gene

KAT6B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.3 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei815 – 8151By similarity
    Active sitei857 – 8571NucleophileBy similarity
    Binding sitei895 – 8951Acetyl-CoABy similarity
    Sitei1222 – 12232Breakpoint for translocation to form KAT6B-CREBBP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri213 – 27260PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri269 – 32052PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri749 – 77123C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. acetyltransferase activity Source: UniProtKB
    2. DNA binding Source: InterPro
    3. histone acetyltransferase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. transcription factor binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone acetylation Source: UniProtKB
    3. histone H3 acetylation Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. nucleosome assembly Source: UniProtKB
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.3.1.48. 2681.
    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase KAT6B (EC:2.3.1.48)
    Alternative name(s):
    Histone acetyltransferase MOZ2
    MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
    Short name:
    MYST-4
    Monocytic leukemia zinc finger protein-related factor
    Gene namesi
    Name:KAT6B
    Synonyms:KIAA0383, MORF, MOZ2, MYST4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17582. KAT6B.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleosome Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving KAT6B may be a cause acute myeloid leukemias. Translocation t(10;16)(q22;p13) with CREBBP.
    Ohdo syndrome, SBBYS variant (SBBYSS) [MIM:603736]: A syndrome characterized by distinctive facial appearance with severe blepharophimosis, an immobile mask-like face, a bulbous nasal tip, and a small mouth with a thin upper lip. The condition presents in infancy with severe hypotonia and feeding problems. Associated skeletal problems include joint laxity, abnormally long thumbs and great toes, and dislocated or hypoplastic patellae. Structural cardiac defects are present in around 50% of cases, and dental anomalies, including small and pointed teeth, are common. Optic atrophy and conductive or sensorineural deafness are repeatedly reported. Many affected individuals have abnormalities of thyroid structure or function. SBBYSS is usually associated with severe mental retardation, delayed motor milestones, and significantly impaired speech.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Genitopatellar syndrome (GTPTS) [MIM:606170]: A rare disorder consisting of microcephaly, severe psychomotor retardation, and characteristic coarse facial features, including broad nose and small or retracted chin, associated with congenital flexion contractures of the lower extremities, abnormal or missing patellae, and urogenital anomalies.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi603736. phenotype.
    606170. phenotype.
    Orphaneti3047. Blepharophimosis-intellectual disability syndrome, SBBYS type.
    85201. Genitopatellar syndrome.
    648. Noonan syndrome.
    PharmGKBiPA134880712.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20732073Histone acetyltransferase KAT6BPRO_0000051575Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei815 – 8151N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei1038 – 10381N6-acetyllysine1 Publication
    Modified residuei1042 – 10421N6-acetyllysine1 Publication
    Modified residuei1044 – 10441N6-acetyllysine1 Publication

    Post-translational modificationi

    Autoacetylated.
    Autoacetylation at Lys-815 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8WYB5.
    PaxDbiQ8WYB5.
    PRIDEiQ8WYB5.

    PTM databases

    PhosphoSiteiQ8WYB5.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with high levels in heart, pancreas, testis and ovary.1 Publication

    Gene expression databases

    ArrayExpressiQ8WYB5.
    BgeeiQ8WYB5.
    CleanExiHS_MYST4.
    GenevestigatoriQ8WYB5.

    Organism-specific databases

    HPAiHPA006104.

    Interactioni

    Subunit structurei

    Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1 and RUNX2.3 Publications

    Protein-protein interaction databases

    BioGridi117069. 10 interactions.
    IntActiQ8WYB5. 3 interactions.
    MINTiMINT-2871056.
    STRINGi9606.ENSP00000287239.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WYB5.
    SMRiQ8WYB5. Positions 211-320, 718-990.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini103 – 17674H15PROSITE-ProRule annotationAdd
    BLAST
    Domaini715 – 989275MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni361 – 717357Negatively regulates HAT activityAdd
    BLAST
    Regioni718 – 1008291CatalyticAdd
    BLAST
    Regioni752 – 1008257Interaction with BRPF1Add
    BLAST
    Regioni856 – 8605Acetyl-CoA bindingBy similarity
    Regioni865 – 8717Acetyl-CoA bindingBy similarity
    Regioni1560 – 2073514Interaction with RUNX1 and RUNX2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi492 – 53342Ser-richAdd
    BLAST
    Compositional biasi521 – 5244Poly-Ser
    Compositional biasi599 – 6057Poly-Ser
    Compositional biasi1070 – 110435Poly-GluAdd
    BLAST
    Compositional biasi1204 – 12074Poly-Glu
    Compositional biasi1351 – 137323Poly-GluAdd
    BLAST
    Compositional biasi1409 – 14179Poly-Glu
    Compositional biasi1594 – 1763170Ser-richAdd
    BLAST
    Compositional biasi1961 – 2061101Met-richAdd
    BLAST

    Domaini

    The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.1 Publication

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 C2HC-type zinc finger.Curated
    Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
    Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri213 – 27260PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri269 – 32052PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri749 – 77123C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5027.
    HOVERGENiHBG052563.
    InParanoidiQ8WYB5.
    KOiK11306.
    OMAiLRWTPIL.
    OrthoDBiEOG7WHH8N.
    PhylomeDBiQ8WYB5.
    TreeFamiTF106483.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.30.40.10. 1 hit.
    3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR005818. Histone_H1/H5_H15.
    IPR002717. MOZ_SAS.
    IPR011991. WHTH_DNA-bd_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00538. Linker_histone. 1 hit.
    PF01853. MOZ_SAS. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00526. H15. 1 hit.
    SM00249. PHD. 2 hits.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS51504. H15. 1 hit.
    PS51726. MYST_HAT. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WYB5-1) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ     50
    LELSVQDGSV LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN 100
    DLRNVDWNKL LRRAIEGLEE PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ 150
    RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD GKGAPQYPSA FPSSLPPVSL 200
    LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC GSSGHPSCLK 250
    FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC 300
    DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK 350
    QRLLSVTSDE GSMNAFTGRG SPGRGQKTKV CTTPSSGHAA SGKDSSSRLA 400
    VTDPTRPGAT TKITTTSTYI SASTLKVNKK TKGLIDGLTK FFTPSPDGRR 450
    SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA TGTTQKLKPP PSSLPPPTPI 500
    SGQSPSSQKS STATSSPSPQ SSSSQCSVPS LSSLTTNSQL KALFDGLSHI 550
    YTTQGQSRKK GHPSYAPPKR MRRKTELSST AKSKAHFFGK RDIRSRFISH 600
    SSSSSWGMAR GSIFKAIAHF KRTTFLKKHR MLGRLKYKVT PQMGTPSPGK 650
    GSLTDGRIKP DQDDDTEIKI NIKQESADVN VIGNKDVVTE EDLDVFKQAQ 700
    ELSWEKIECE SGVEDCGRYP SVIEFGKYEI QTWYSSPYPQ EYARLPKLYL 750
    CEFCLKYMKS KNILLRHSKK CGWFHPPANE IYRRKDLSVF EVDGNMSKIY 800
    CQNLCLLAKL FLDHKTLYYD VEPFLFYVLT KNDEKGCHLV GYFSKEKLCQ 850
    QKYNVSCIMI MPQHQRQGFG RFLIDFSYLL SRREGQAGSP EKPLSDLGRL 900
    SYLAYWKSVI LEYLYHHHER HISIKAISRA TGMCPHDIAT TLQHLHMIDK 950
    RDGRFVIIRR EKLILSHMEK LKTCSRANEL DPDSLRWTPI LISNAAVSEE 1000
    EREAEKEAER LMEQASCWEK EEQEILSTRA NSRQSPAKVQ SKNKYLHSPE 1050
    SRPVTGERGQ LLELSKESSE EEEEEEDEEE EEEEEEEEED EEEEEEEEEE 1100
    EEEENIQSSP PRLTKPQSVA IKRKRPFVLK KKRGRKRRRI NSSVTTETIS 1150
    ETTEVLNEPF DNSDEERPMP QLEPTCEIEV EEDGRKPVLR KAFQHQPGKK 1200
    RQTEEEEGKD NHCFKNADPC RNNMNDDSSN LKEGSKDNPE PLKCKQVWPK 1250
    GTKRGLSKWR QNKERKTGFK LNLYTPPETP MEPDEQVTVE EQKETSEGKT 1300
    SPSPIRIEEE VKETGEALLP QEENRREETC APVSPNTSPG EKPEDDLIKP 1350
    EEEEEEEEEE EEEEEEEEGE EEEGGGNVEK DPDGAKSQEK EEPEISTEKE 1400
    DSARLDDHEE EEEEDEEPSH NEDHDADDED DSHMESAEVE KEELPRESFK 1450
    EVLENQETFL DLNVQPGHSN PEVLMDCGVD LTASCNSEPK ELAGDPEAVP 1500
    ESDEEPPPGE QAQKQDQKNS KEVDTEFKEG NPATMEIDSE TVQAVQSLTQ 1550
    ESSEQDDTFQ DCAETQEACR SLQNYTRADQ SPQIATTLDD CQQSDHSSPV 1600
    SSVHSHPGQS VRSVNSPSVP ALENSYAQIS PDQSAISVPS LQNMETSPMM 1650
    DVPSVSDHSQ QVVDSGFSDL GSIESTTENY ENPSSYDSTM GGSICGNGSS 1700
    QNSCSYSNLT SSSLTQSSCA VTQQMSNISG SCSMLQQTSI SSPPTCSVKS 1750
    PQGCVVERPP SSSQQLAQCS MAANFTPPMQ LAEIPETSNA NIGLYERMGQ 1800
    SDFGAGHYPQ PSATFSLAKL QQLTNTLIDH SLPYSHSAAV TSYANSASLS 1850
    TPLSNTGLVQ LSQSPHSVPG GPQAQATMTP PPNLTPPPMN LPPPLLQRNM 1900
    AASNIGISHS QRLQTQIASK GHISMRTKSA SLSPAAATHQ SQIYGRSQTV 1950
    AMQGPARTLT MQRGMNMSVN LMPAPAYNVN SVNMNMNTLN AMNGYSMSQP 2000
    MMNSGYHSNH GYMNQTPQYP MQMQMGMMGT QPYAQQPMQT PPHGNMMYTA 2050
    PGHHGYMNTG MSKQSLNGSY MRR 2073
    Length:2,073
    Mass (Da):231,378
    Last modified:April 3, 2007 - v3
    Checksum:iAEE267B9DA444B08
    GO
    Isoform 2 (identifier: Q8WYB5-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         482-664: Missing.

    Show »
    Length:1,890
    Mass (Da):211,537
    Checksum:i9AD95D653693CFBA
    GO
    Isoform 3 (identifier: Q8WYB5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         373-664: Missing.

    Show »
    Length:1,781
    Mass (Da):199,858
    Checksum:i895F7DE8B12455E8
    GO

    Sequence cautioni

    The sequence AAH14143.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH48199.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAF00100.1 differs from that shown. Reason: Frameshift at positions 550 and 562.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti123 – 1231G → R in AAL56647. 1 PublicationCurated
    Sequence conflicti231 – 2311P → A in AAL56647. 1 PublicationCurated
    Sequence conflicti843 – 8431F → L in AAF00095. (PubMed:10497217)Curated
    Sequence conflicti843 – 8431F → L in AAF00099. (PubMed:10497217)Curated
    Sequence conflicti843 – 8431F → L in AAF00100. (PubMed:10497217)Curated
    Sequence conflicti843 – 8431F → L in BAA20837. (PubMed:9205841)Curated
    Sequence conflicti931 – 9333TGM → RHV in AAL56647. 1 PublicationCurated
    Sequence conflicti934 – 9341Missing in AAL56647. 1 PublicationCurated
    Sequence conflicti1152 – 11521T → S in AAL56647. 1 PublicationCurated
    Sequence conflicti1625 – 16251S → T in AAL56647. 1 PublicationCurated
    Sequence conflicti1731 – 17311S → T in AAL56647. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti360 – 3601E → K.1 Publication
    VAR_067315
    Natural varianti483 – 4831T → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036361
    Natural varianti1217 – 12171A → S.
    Corresponds to variant rs57372986 [ dbSNP | Ensembl ].
    VAR_061367
    Natural varianti1499 – 14991V → I.
    Corresponds to variant rs3740321 [ dbSNP | Ensembl ].
    VAR_050217

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei373 – 664292Missing in isoform 3. 2 PublicationsVSP_014586Add
    BLAST
    Alternative sequencei482 – 664183Missing in isoform 2. 1 PublicationVSP_014587Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113514 mRNA. Translation: AAF00095.1.
    AF119230 mRNA. Translation: AAF00099.1.
    AF119231 mRNA. Translation: AAF00100.1. Frameshift.
    AF217500 mRNA. Translation: AAL56647.1.
    AB002381 mRNA. Translation: BAA20837.2.
    BC014143 mRNA. Translation: AAH14143.1. Sequence problems.
    BC021128 mRNA. Translation: AAH21128.1.
    BC048199 mRNA. Translation: AAH48199.1. Sequence problems.
    CCDSiCCDS58084.1. [Q8WYB5-3]
    CCDS58085.1. [Q8WYB5-2]
    CCDS7345.1. [Q8WYB5-1]
    RefSeqiNP_001243397.1. NM_001256468.1. [Q8WYB5-2]
    NP_001243398.1. NM_001256469.1. [Q8WYB5-3]
    NP_036462.2. NM_012330.3. [Q8WYB5-1]
    XP_005269721.1. XM_005269664.1. [Q8WYB5-1]
    UniGeneiHs.35758.
    Hs.599543.
    Hs.740873.

    Genome annotation databases

    EnsembliENST00000287239; ENSP00000287239; ENSG00000156650. [Q8WYB5-1]
    ENST00000372711; ENSP00000361796; ENSG00000156650. [Q8WYB5-2]
    ENST00000372714; ENSP00000361799; ENSG00000156650. [Q8WYB5-3]
    ENST00000372724; ENSP00000361809; ENSG00000156650. [Q8WYB5-3]
    ENST00000372725; ENSP00000361810; ENSG00000156650. [Q8WYB5-3]
    GeneIDi23522.
    KEGGihsa:23522.
    UCSCiuc001jwm.2. human. [Q8WYB5-3]
    uc001jwn.2. human. [Q8WYB5-1]
    uc031pvy.1. human. [Q8WYB5-2]

    Polymorphism databases

    DMDMi143811424.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113514 mRNA. Translation: AAF00095.1 .
    AF119230 mRNA. Translation: AAF00099.1 .
    AF119231 mRNA. Translation: AAF00100.1 . Frameshift.
    AF217500 mRNA. Translation: AAL56647.1 .
    AB002381 mRNA. Translation: BAA20837.2 .
    BC014143 mRNA. Translation: AAH14143.1 . Sequence problems.
    BC021128 mRNA. Translation: AAH21128.1 .
    BC048199 mRNA. Translation: AAH48199.1 . Sequence problems.
    CCDSi CCDS58084.1. [Q8WYB5-3 ]
    CCDS58085.1. [Q8WYB5-2 ]
    CCDS7345.1. [Q8WYB5-1 ]
    RefSeqi NP_001243397.1. NM_001256468.1. [Q8WYB5-2 ]
    NP_001243398.1. NM_001256469.1. [Q8WYB5-3 ]
    NP_036462.2. NM_012330.3. [Q8WYB5-1 ]
    XP_005269721.1. XM_005269664.1. [Q8WYB5-1 ]
    UniGenei Hs.35758.
    Hs.599543.
    Hs.740873.

    3D structure databases

    ProteinModelPortali Q8WYB5.
    SMRi Q8WYB5. Positions 211-320, 718-990.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117069. 10 interactions.
    IntActi Q8WYB5. 3 interactions.
    MINTi MINT-2871056.
    STRINGi 9606.ENSP00000287239.

    PTM databases

    PhosphoSitei Q8WYB5.

    Polymorphism databases

    DMDMi 143811424.

    Proteomic databases

    MaxQBi Q8WYB5.
    PaxDbi Q8WYB5.
    PRIDEi Q8WYB5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287239 ; ENSP00000287239 ; ENSG00000156650 . [Q8WYB5-1 ]
    ENST00000372711 ; ENSP00000361796 ; ENSG00000156650 . [Q8WYB5-2 ]
    ENST00000372714 ; ENSP00000361799 ; ENSG00000156650 . [Q8WYB5-3 ]
    ENST00000372724 ; ENSP00000361809 ; ENSG00000156650 . [Q8WYB5-3 ]
    ENST00000372725 ; ENSP00000361810 ; ENSG00000156650 . [Q8WYB5-3 ]
    GeneIDi 23522.
    KEGGi hsa:23522.
    UCSCi uc001jwm.2. human. [Q8WYB5-3 ]
    uc001jwn.2. human. [Q8WYB5-1 ]
    uc031pvy.1. human. [Q8WYB5-2 ]

    Organism-specific databases

    CTDi 23522.
    GeneCardsi GC10P076586.
    GeneReviewsi KAT6B.
    HGNCi HGNC:17582. KAT6B.
    HPAi HPA006104.
    MIMi 603736. phenotype.
    605880. gene.
    606170. phenotype.
    neXtProti NX_Q8WYB5.
    Orphaneti 3047. Blepharophimosis-intellectual disability syndrome, SBBYS type.
    85201. Genitopatellar syndrome.
    648. Noonan syndrome.
    PharmGKBi PA134880712.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5027.
    HOVERGENi HBG052563.
    InParanoidi Q8WYB5.
    KOi K11306.
    OMAi LRWTPIL.
    OrthoDBi EOG7WHH8N.
    PhylomeDBi Q8WYB5.
    TreeFami TF106483.

    Enzyme and pathway databases

    BRENDAi 2.3.1.48. 2681.
    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi KAT6B. human.
    GeneWikii MYST4.
    GenomeRNAii 23522.
    NextBioi 45977.
    PROi Q8WYB5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WYB5.
    Bgeei Q8WYB5.
    CleanExi HS_MYST4.
    Genevestigatori Q8WYB5.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.30.40.10. 1 hit.
    3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR005818. Histone_H1/H5_H15.
    IPR002717. MOZ_SAS.
    IPR011991. WHTH_DNA-bd_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00538. Linker_histone. 1 hit.
    PF01853. MOZ_SAS. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00526. H15. 1 hit.
    SM00249. PHD. 2 hits.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS51504. H15. 1 hit.
    PS51726. MYST_HAT. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein."
      Champagne N., Bertos N.R., Pelletier N., Wang A.H., Vezmar M., Yang Y., Heng H.H., Yang X.-J.
      J. Biol. Chem. 274:28528-28536(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, ACETYLATION, ENZYME ACTIVITY, DOMAIN, FUNCTION.
      Tissue: Bone marrow.
    2. "Structure and function of the human MYST family: MOZ2, MYST1 and MYST2."
      Borrow J., Housman D.E.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322 AND 1187-2073.
      Tissue: Brain and Lung.
    6. "Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13)."
      Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U., Billstroem R., Stroembeck B., Mitelman F., Johansson B.
      Hum. Mol. Genet. 10:395-404(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1136-1287, CHROMOSOMAL TRANSLOCATION WITH CREBBP.
    7. "MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2."
      Pelletier N., Champagne N., Stifani S., Yang X.-J.
      Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RUNX1 AND RUNX2, ACETYLATION, FUNCTION.
    8. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
    9. Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1038; LYS-1042 AND LYS-1044, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Whole-exome-sequencing identifies mutations in histone acetyltransferase gene KAT6B in individuals with the Say-Barber-Biesecker variant of Ohdo syndrome."
      Clayton-Smith J., O'Sullivan J., Daly S., Bhaskar S., Day R., Anderson B., Voss A.K., Thomas T., Biesecker L.G., Smith P., Fryer A., Chandler K.E., Kerr B., Tassabehji M., Lynch S.A., Krajewska-Walasek M., McKee S., Smith J.
      , Sweeney E., Mansour S., Mohammed S., Donnai D., Black G.
      Am. J. Hum. Genet. 89:675-681(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SBBYSS, VARIANT LYS-360.
    12. Cited for: INVOLVEMENT IN GTPTS.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-483.

    Entry informationi

    Entry nameiKAT6B_HUMAN
    AccessioniPrimary (citable) accession number: Q8WYB5
    Secondary accession number(s): O15087
    , Q86Y05, Q8WU81, Q9UKW2, Q9UKW3, Q9UKX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3